Copper-binding motifs Xxx-His or Xxx-Zzz-His (ATCUN) linked to an antimicrobial peptide: Cu-binding, antimicrobial activity and ROS production.

Antimicrobial peptide Copper Metallopeptide N-terminal Cu(II) binding site Reactive oxygen species Redox

Journal

Journal of inorganic biochemistry
ISSN: 1873-3344
Titre abrégé: J Inorg Biochem
Pays: United States
ID NLM: 7905788

Informations de publication

Date de publication:
12 2020
Historique:
received: 19 05 2020
revised: 28 08 2020
accepted: 06 09 2020
pubmed: 28 9 2020
medline: 13 7 2021
entrez: 27 9 2020
Statut: ppublish

Résumé

Depending on the coordination, copper ions can have a very high activity in catalyzing the production of reactive oxygen species. Thus interest arose in increasing the activity of antimicrobial peptides (AMPs) by equipping them with a Cu-binding unit. Several examples, native and engineered, have been investigated with the motif Xxx-Zzz-His, called Amino Terminal Cu(II)- and Ni(II)-binding (ATCUN) motif. Here we investigate a short AMP that was equipped either with Xxx-Zzz-His or Xxx-His. Xxx-His is a shorter motif and yields a more redox active copper complex. The control AMP, Xxx-His-AMP and Xxx-Zzz-His-AMP were investigated toward Cu-binding, Reactive Oxygen Species (ROS) production and antimicrobial activity in E. coli. The data indicate that these Cu-binding motifs have very limited impact on antimicrobial activity and low ROS production capability.

Identifiants

pubmed: 32980641
pii: S0162-0134(20)30283-X
doi: 10.1016/j.jinorgbio.2020.111255
pii:
doi:

Substances chimiques

Amino Acids 0
Pore Forming Cytotoxic Proteins 0
Reactive Oxygen Species 0
Copper 789U1901C5

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

111255

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Auteurs

Merwan Bouraguba (M)

Biometals and Biological Chemistry, Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67 000 Strasbourg, France.

Elise Glattard (E)

Membrane Biophysics and NMR, Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67 000 Strasbourg, France.

Maxime Naudé (M)

Biometals and Biological Chemistry, Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67 000 Strasbourg, France.

Rémi Pelletier (R)

Biometals and Biological Chemistry, Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67 000 Strasbourg, France.

Christopher Aisenbrey (C)

Membrane Biophysics and NMR, Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67 000 Strasbourg, France.

Burkhard Bechinger (B)

Membrane Biophysics and NMR, Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67 000 Strasbourg, France; Institut Universitaire de France, France.

Laurent Raibaut (L)

Biometals and Biological Chemistry, Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67 000 Strasbourg, France.

Vincent Lebrun (V)

Biometals and Biological Chemistry, Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67 000 Strasbourg, France. Electronic address: vlebrun@unistra.fr.

Peter Faller (P)

Biometals and Biological Chemistry, Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67 000 Strasbourg, France. Electronic address: pfaller@unistra.fr.

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